δ-Aminolevulinate dehydratase, a zinc dependent enzyme
Erythrocyte and liver tissue δ-aminolevulinate dehydratase activity was determined in rats fed a semipurified diet under controlled nutritional intake of zinc and copper. A significant decrease in enzymatic activity was observed in animals fed low zinc diet, while dietary copper had no effect. In vi...
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| Veröffentlicht in: | Biochemical and biophysical research communications 1974-10, Vol.60 (4), p.1418-1424 |
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| container_title | Biochemical and biophysical research communications |
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| creator | Finelli, V.N. Murthy, L. Peirano, W.B. Petering, H.G. |
| description | Erythrocyte and liver tissue δ-aminolevulinate dehydratase activity was determined in rats fed a semipurified diet under controlled nutritional intake of zinc and copper. A significant decrease in enzymatic activity was observed in animals fed low zinc diet, while dietary copper had no effect.
In vitro
addition of zinc to the erythrocyte preparations obtained from rats on low zinc diet produced a slight increase in enzymatic activity. It appears that, even though zinc may be the metal ion activator of δ-aminolevulinate dehydratase, the requirement of this metal is at the site of synthesis of this enzyme. |
| doi_str_mv | 10.1016/0006-291X(74)90356-8 |
| format | Article |
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In vitro
addition of zinc to the erythrocyte preparations obtained from rats on low zinc diet produced a slight increase in enzymatic activity. It appears that, even though zinc may be the metal ion activator of δ-aminolevulinate dehydratase, the requirement of this metal is at the site of synthesis of this enzyme.</description><identifier>ISSN: 0006-291X</identifier><identifier>EISSN: 1090-2104</identifier><identifier>DOI: 10.1016/0006-291X(74)90356-8</identifier><identifier>PMID: 4417495</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Animals ; Copper - pharmacology ; Enzyme Activation - drug effects ; Erythrocytes - drug effects ; Erythrocytes - enzymology ; Female ; Humans ; Hydro-Lyases - metabolism ; Kinetics ; Liver - drug effects ; Liver - enzymology ; Male ; Organ Specificity ; Porphobilinogen Synthase - antagonists & inhibitors ; Porphobilinogen Synthase - blood ; Porphobilinogen Synthase - metabolism ; Rats ; Species Specificity ; Zinc - pharmacology</subject><ispartof>Biochemical and biophysical research communications, 1974-10, Vol.60 (4), p.1418-1424</ispartof><rights>1974</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c357t-89e5e053f2e1419ffdee051ce8f27b59a399248eef59e4425fd3d96f5c1114a13</citedby><cites>FETCH-LOGICAL-c357t-89e5e053f2e1419ffdee051ce8f27b59a399248eef59e4425fd3d96f5c1114a13</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/0006-291X(74)90356-8$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/4417495$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Finelli, V.N.</creatorcontrib><creatorcontrib>Murthy, L.</creatorcontrib><creatorcontrib>Peirano, W.B.</creatorcontrib><creatorcontrib>Petering, H.G.</creatorcontrib><title>δ-Aminolevulinate dehydratase, a zinc dependent enzyme</title><title>Biochemical and biophysical research communications</title><addtitle>Biochem Biophys Res Commun</addtitle><description>Erythrocyte and liver tissue δ-aminolevulinate dehydratase activity was determined in rats fed a semipurified diet under controlled nutritional intake of zinc and copper. A significant decrease in enzymatic activity was observed in animals fed low zinc diet, while dietary copper had no effect.
In vitro
addition of zinc to the erythrocyte preparations obtained from rats on low zinc diet produced a slight increase in enzymatic activity. It appears that, even though zinc may be the metal ion activator of δ-aminolevulinate dehydratase, the requirement of this metal is at the site of synthesis of this enzyme.</description><subject>Animals</subject><subject>Copper - pharmacology</subject><subject>Enzyme Activation - drug effects</subject><subject>Erythrocytes - drug effects</subject><subject>Erythrocytes - enzymology</subject><subject>Female</subject><subject>Humans</subject><subject>Hydro-Lyases - metabolism</subject><subject>Kinetics</subject><subject>Liver - drug effects</subject><subject>Liver - enzymology</subject><subject>Male</subject><subject>Organ Specificity</subject><subject>Porphobilinogen Synthase - antagonists & inhibitors</subject><subject>Porphobilinogen Synthase - blood</subject><subject>Porphobilinogen Synthase - metabolism</subject><subject>Rats</subject><subject>Species Specificity</subject><subject>Zinc - pharmacology</subject><issn>0006-291X</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1974</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kN1KwzAUx4Moc07fQKFXomA1SZO2uRmM4RcMvFHwLmTJCUbadCbtYHsun8NnsnNjl14dzvn_z9cPoXOCbwkm-R3GOE-pIO9XBbsWOON5Wh6gIcECp5RgdoiGe8sxOonxE2NCWC4GaMAYKZjgQ1T8fKeT2vmmgmVXOa9aSAx8rExQrYpwk6hk7bzuawvwBnybgF-vajhFR1ZVEc52cYTeHu5fp0_p7OXxeTqZpTrjRZuWAjhgnlkKhBFhrYE-JRpKS4s5FyoTgrISwHIBjFFuTWZEbrkm_amKZCN0uZ27CM1XB7GVtYsaqkp5aLooS8pxKTjtjWxr1KGJMYCVi-BqFVaSYLnhJTcw5AaGLJj84yXLvu1iN7-b12D2TTtAvT7e6tA_uXQQZNQOvAbjAuhWmsb9v-AXKQN6OA</recordid><startdate>19741023</startdate><enddate>19741023</enddate><creator>Finelli, V.N.</creator><creator>Murthy, L.</creator><creator>Peirano, W.B.</creator><creator>Petering, H.G.</creator><general>Elsevier Inc</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>19741023</creationdate><title>δ-Aminolevulinate dehydratase, a zinc dependent enzyme</title><author>Finelli, V.N. ; Murthy, L. ; Peirano, W.B. ; Petering, H.G.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c357t-89e5e053f2e1419ffdee051ce8f27b59a399248eef59e4425fd3d96f5c1114a13</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1974</creationdate><topic>Animals</topic><topic>Copper - pharmacology</topic><topic>Enzyme Activation - drug effects</topic><topic>Erythrocytes - drug effects</topic><topic>Erythrocytes - enzymology</topic><topic>Female</topic><topic>Humans</topic><topic>Hydro-Lyases - metabolism</topic><topic>Kinetics</topic><topic>Liver - drug effects</topic><topic>Liver - enzymology</topic><topic>Male</topic><topic>Organ Specificity</topic><topic>Porphobilinogen Synthase - antagonists & inhibitors</topic><topic>Porphobilinogen Synthase - blood</topic><topic>Porphobilinogen Synthase - metabolism</topic><topic>Rats</topic><topic>Species Specificity</topic><topic>Zinc - pharmacology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Finelli, V.N.</creatorcontrib><creatorcontrib>Murthy, L.</creatorcontrib><creatorcontrib>Peirano, W.B.</creatorcontrib><creatorcontrib>Petering, H.G.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Biochemical and biophysical research communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Finelli, V.N.</au><au>Murthy, L.</au><au>Peirano, W.B.</au><au>Petering, H.G.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>δ-Aminolevulinate dehydratase, a zinc dependent enzyme</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>1974-10-23</date><risdate>1974</risdate><volume>60</volume><issue>4</issue><spage>1418</spage><epage>1424</epage><pages>1418-1424</pages><issn>0006-291X</issn><eissn>1090-2104</eissn><abstract>Erythrocyte and liver tissue δ-aminolevulinate dehydratase activity was determined in rats fed a semipurified diet under controlled nutritional intake of zinc and copper. A significant decrease in enzymatic activity was observed in animals fed low zinc diet, while dietary copper had no effect.
In vitro
addition of zinc to the erythrocyte preparations obtained from rats on low zinc diet produced a slight increase in enzymatic activity. It appears that, even though zinc may be the metal ion activator of δ-aminolevulinate dehydratase, the requirement of this metal is at the site of synthesis of this enzyme.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>4417495</pmid><doi>10.1016/0006-291X(74)90356-8</doi><tpages>7</tpages></addata></record> |
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| ispartof | Biochemical and biophysical research communications, 1974-10, Vol.60 (4), p.1418-1424 |
| issn | 0006-291X 1090-2104 |
| language | eng |
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| source | MEDLINE; Elsevier ScienceDirect Journals Complete |
| subjects | Animals Copper - pharmacology Enzyme Activation - drug effects Erythrocytes - drug effects Erythrocytes - enzymology Female Humans Hydro-Lyases - metabolism Kinetics Liver - drug effects Liver - enzymology Male Organ Specificity Porphobilinogen Synthase - antagonists & inhibitors Porphobilinogen Synthase - blood Porphobilinogen Synthase - metabolism Rats Species Specificity Zinc - pharmacology |
| title | δ-Aminolevulinate dehydratase, a zinc dependent enzyme |
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